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Author |
Connor, R.J.; Kawaoka, Y.; Webster, R.G.; Paulson, J.C. |
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Title |
Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates |
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Journal Article |
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Year |
1994 |
Publication |
Virology |
Abbreviated Journal |
Virology |
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Volume |
205 |
Issue |
1 |
Pages |
17-23 |
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Keywords |
Amino Acid Sequence; Amino Acids/genetics; Animals; Carbohydrate Sequence; Chick Embryo; Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinins, Viral/genetics; Influenza A virus/*metabolism; Molecular Sequence Data; Receptors, Virus/*metabolism; Species Specificity; Viral Envelope Proteins/genetics |
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Abstract |
The receptor specificity of 56 H2 and H3 influenza virus isolates from various animal species has been determined to test the relevance of receptor specificity to the ecology of influenza virus. The results show that the receptor specificity of both H2 and H3 isolates evaluated for sialic acid linkage specificity and inhibition of hemagglutination by horse serum correlates with the species of origin, as postulated earlier for H3 strains based on a limited survey of five human, three avian, and one equine strain. Elucidation of the amino acid sequence of several human H2 receptor variants and analysis of known sequences of H2 and H3 isolates revealed that receptor specificity varies in association with an amino acid change at residues 228 in addition to the change at residue 226 previously documented to affect receptor specificity of H3 but not H1 isolates. Residues 226 and 228 are leucine and serine in human isolates, which preferentially bind sialic acid alpha 2,6-galactose beta 1,4-N-acetyl glucosamine (SA alpha 2,6Gal), and glutamine and glycine in avian and equine isolates, which exhibit specificity for sialic acid alpha-2,3-galactose beta-1,3-N-acetyl galactosamine (SA alpha 2,3Gal). The results demonstrate that the correlation of receptor specificity and species of origin is maintained across both H2 and H3 influenza virus serotypes and provide compelling evidence that influenza virus hosts exert selective pressure to maintain the receptor specificity characteristics of strains isolated from that species. |
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Department of Biological Chemistry, UCLA School of Medicine 90024-1737 |
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English |
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Series Volume |
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0042-6822 |
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Notes |
PMID:7975212 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
2662 |
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Author |
Dowdle, W.R.; Schild, G.C. |
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Title |
Influenza: its antigenic variation and ecology |
Type |
Journal Article |
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Year |
1976 |
Publication |
Bulletin of the Pan American Health Organization |
Abbreviated Journal |
Bull Pan Am Health Organ |
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Volume |
10 |
Issue |
3 |
Pages |
193-195 |
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Keywords |
Animals; *Antigens, Viral; Bird Diseases/microbiology; Birds; Hemagglutinins, Viral; Horse Diseases/microbiology; Horses; Humans; Influenza A virus/immunology/isolation & purification; Influenza, Human/epidemiology; Mutation; Neuraminidase/immunology; Orthomyxoviridae/enzymology/*immunology; Orthomyxoviridae Infections/microbiology/veterinary; Recombination, Genetic; Swine; Swine Diseases/microbiology |
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Abstract |
Influenza viruses have two surface antigens, the glycoprotein structures hemagglutinin (HA) and neuraminidase (NA). Antibodies to each of these are associated with immunity, but the structures themselves are antigenically variable. When an antigenic change is gradual over time it is referred to as a drift, while a sudden complete or major change in either or both antigens is termed a shift. The mechanism of antigenic drift is usually attributed to selection of preexisting mutants by pressure from increasing immunity in the human population. The mechanism of antigenic shift is less clear, but one tentative hypothesis is that shifts arise from mammalian or avian reservoirs, or through genetic recombination of human and animal influenza strains. |
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English |
Summary Language |
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0085-4638 |
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Notes |
PMID:187273 |
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Call Number |
Equine Behaviour @ team @ |
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2700 |
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